REEP1_HUMAN
ID REEP1_HUMAN Reviewed; 201 AA.
AC Q9H902; B7Z4D7; B7Z4F2; B7Z5R9; D6W5M2; Q53TI0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Receptor expression-enhancing protein 1;
DE AltName: Full=Spastic paraplegia 31 protein {ECO:0000303|PubMed:23969831};
GN Name=REEP1; Synonyms=C2orf23, SPG31 {ECO:0000303|PubMed:23969831};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT "RTP family members induce functional expression of mammalian odorant
RT receptors.";
RL Cell 119:679-691(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16720576; DOI=10.1074/jbc.m513637200;
RA Behrens M., Bartelt J., Reichling C., Winnig M., Kuhn C., Meyerhof W.;
RT "Members of RTP and REEP gene families influence functional bitter taste
RT receptor expression.";
RL J. Biol. Chem. 281:20650-20659(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST; ATL1 AND
RP MICROTUBULES.
RX PubMed=20200447; DOI=10.1172/jci40979;
RA Park S.H., Zhu P.P., Parker R.L., Blackstone C.;
RT "Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1
RT coordinate microtubule interactions with the tubular ER network.";
RL J. Clin. Invest. 120:1097-1110(2010).
RN [10]
RP INVOLVEMENT IN HMN5B, AND CHARACTERIZATION OF VARIANT SPG31 GLU-20.
RX PubMed=22703882; DOI=10.1016/j.ajhg.2012.05.007;
RA Beetz C., Pieber T.R., Hertel N., Schabhuttl M., Fischer C., Trajanoski S.,
RA Graf E., Keiner S., Kurth I., Wieland T., Varga R.E., Timmerman V.,
RA Reilly M.M., Strom T.M., Auer-Grumbach M.;
RT "Exome sequencing identifies a REEP1 mutation involved in distal hereditary
RT motor neuropathy type V.";
RL Am. J. Hum. Genet. 91:139-145(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP INTERACTION WITH ZFYVE27.
RX PubMed=23969831; DOI=10.1073/pnas.1307391110;
RA Chang J., Lee S., Blackstone C.;
RT "Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and
RT regulates network formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013).
RN [13]
RP FUNCTION, VARIANT SPG31 ARG-19, VARIANT LYS-55, CHARACTERIZATION OF
RP VARIANTS SPG31 ARG-19; LEU-19; GLU-20; PHE-23; ARG-42 AND ASN-56, AND
RP CHARACTERIZATION OF VARIANT LYS-55.
RX PubMed=24478229; DOI=10.1002/humu.22521;
RA Falk J., Rohde M., Bekhite M.M., Neugebauer S., Hemmerich P., Kiehntopf M.,
RA Deufel T., Huebner C.A., Beetz C.;
RT "Functional mutation analysis provides evidence for a role of REEP1 in
RT lipid droplet biology.";
RL Hum. Mutat. 35:497-504(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANTS SPG31 LYS-55 AND PRO-107.
RX PubMed=18644145; DOI=10.1186/1471-2350-9-71;
RA Schlang K.J., Arning L., Epplen J.T., Stemmler S.;
RT "Autosomal dominant hereditary spastic paraplegia: novel mutations in the
RT REEP1 gene (SPG31).";
RL BMC Med. Genet. 9:71-71(2008).
RN [16]
RP VARIANT SPG31 GLU-20, AND SUBCELLULAR LOCATION.
RX PubMed=16826527; DOI=10.1086/505361;
RA Zuechner S., Wang G., Tran-Viet K.-N., Nance M.A., Gaskell P.C.,
RA Vance J.M., Ashley-Koch A.E., Pericak-Vance M.A.;
RT "Mutations in the novel mitochondrial protein REEP1 cause hereditary
RT spastic paraplegia type 31.";
RL Am. J. Hum. Genet. 79:365-369(2006).
RN [17]
RP VARIANT SPG31 GLU-20.
RX PubMed=20718791; DOI=10.1111/j.1399-0004.2010.01501.x;
RA McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A.,
RA Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.;
RT "Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic
RT paraplegia.";
RL Clin. Genet. 79:523-530(2011).
RN [18]
RP VARIANTS SPG31 LEU-19; PHE-23; ARG-42 AND ASN-56.
RX PubMed=21618648; DOI=10.1002/humu.21542;
RA Goizet C., Depienne C., Benard G., Boukhris A., Mundwiller E., Sole G.,
RA Coupry I., Pilliod J., Martin-Negrier M.L., Fedirko E., Forlani S.,
RA Cazeneuve C., Hannequin D., Charles P., Feki I., Pinel J.F.,
RA Ouvrard-Hernandez A.M., Lyonnet S., Ollagnon-Roman E., Yaouanq J.,
RA Toutain A., Dussert C., Fontaine B., Leguern E., Lacombe D., Durr A.,
RA Rossignol R., Brice A., Stevanin G.;
RT "REEP1 mutations in SPG31: frequency, mutational spectrum, and potential
RT association with mitochondrial morpho-functional dysfunction.";
RL Hum. Mutat. 32:1118-1127(2011).
CC -!- FUNCTION: Required for endoplasmic reticulum (ER) network formation,
CC shaping and remodeling; it links ER tubules to the cytoskeleton. May
CC also enhance the cell surface expression of odorant receptors
CC (PubMed:20200447). May play a role in long-term axonal maintenance
CC (PubMed:24478229). {ECO:0000269|PubMed:20200447,
CC ECO:0000269|PubMed:24478229}.
CC -!- SUBUNIT: Interacts with SPAST and ATL1; it preferentially interacts
CC with SPAST isoform 1 (PubMed:20200447). Interacts (via C-terminus) with
CC microtubules (PubMed:20200447). Interacts with odorant receptor
CC proteins (By similarity). Interacts with ZFYVE27 (PubMed:23969831).
CC {ECO:0000250|UniProtKB:Q8BGH4, ECO:0000269|PubMed:20200447,
CC ECO:0000269|PubMed:23969831}.
CC -!- INTERACTION:
CC Q9H902; P78369: CLDN10; NbExp=3; IntAct=EBI-1644241, EBI-13372810;
CC Q9H902; P21291: CSRP1; NbExp=3; IntAct=EBI-1644241, EBI-3959636;
CC Q9H902; O15400: STX7; NbExp=3; IntAct=EBI-1644241, EBI-3221827;
CC Q9H902; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-1644241, EBI-8644968;
CC Q9H902; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-1644241, EBI-12038591;
CC Q9H902; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-1644241, EBI-12111910;
CC Q9H902; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-1644241, EBI-4401271;
CC Q9H902; Q5T4F4: ZFYVE27; NbExp=2; IntAct=EBI-1644241, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:16826527}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:20200447}.
CC Note=Localizes to endoplasmic reticulum tubular network.
CC {ECO:0000269|PubMed:20200447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H902-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H902-2; Sequence=VSP_042573;
CC Name=3;
CC IsoId=Q9H902-3; Sequence=VSP_043251;
CC Name=4;
CC IsoId=Q9H902-4; Sequence=VSP_043252;
CC -!- TISSUE SPECIFICITY: Expressed in circumvallate papillae and testis.
CC {ECO:0000269|PubMed:16720576}.
CC -!- DISEASE: Spastic paraplegia 31, autosomal dominant (SPG31)
CC [MIM:610250]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body.
CC {ECO:0000269|PubMed:16826527, ECO:0000269|PubMed:18644145,
CC ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:21618648,
CC ECO:0000269|PubMed:22703882, ECO:0000269|PubMed:24478229}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Neuronopathy, distal hereditary motor, 5B (HMN5B)
CC [MIM:614751]: A disorder characterized by distal muscular atrophy
CC mainly affecting the upper extremities, in contrast to other distal
CC motor neuronopathies. These constitute a heterogeneous group of
CC neuromuscular diseases caused by selective degeneration of motor
CC neurons in the anterior horn of the spinal cord, without sensory
CC deficit in the posterior horn. The overall clinical picture consists of
CC a classical distal muscular atrophy syndrome in the legs without
CC clinical sensory loss. The disease starts with weakness and wasting of
CC distal muscles of the anterior tibial and peroneal compartments of the
CC legs. Later on, weakness and atrophy may expand to the proximal muscles
CC of the lower limbs and/or to the distal upper limbs. HMN5B is
CC characterized by onset in the first or second decade of distal muscle
CC weakness and atrophy, primarily affecting the intrinsic hand muscles,
CC but also affecting the lower legs, resulting in abnormal gait and pes
CC cavus. {ECO:0000269|PubMed:22703882}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY562239; AAT70684.1; -; mRNA.
DR EMBL; AK023172; BAB14444.1; -; mRNA.
DR EMBL; AK297201; BAH12523.1; -; mRNA.
DR EMBL; AK297287; BAH12538.1; -; mRNA.
DR EMBL; AK299334; BAH13005.1; -; mRNA.
DR EMBL; CR457301; CAG33582.1; -; mRNA.
DR EMBL; AC009408; AAX93132.1; -; Genomic_DNA.
DR EMBL; AC009309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99457.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99458.1; -; Genomic_DNA.
DR EMBL; BC064846; AAH64846.1; -; mRNA.
DR CCDS; CCDS1989.1; -. [Q9H902-1]
DR CCDS; CCDS54372.1; -. [Q9H902-2]
DR CCDS; CCDS54373.1; -. [Q9H902-4]
DR CCDS; CCDS54374.1; -. [Q9H902-3]
DR RefSeq; NP_001158202.1; NM_001164730.1. [Q9H902-3]
DR RefSeq; NP_001158203.1; NM_001164731.1. [Q9H902-2]
DR RefSeq; NP_001158204.1; NM_001164732.1. [Q9H902-4]
DR RefSeq; NP_075063.1; NM_022912.2. [Q9H902-1]
DR AlphaFoldDB; Q9H902; -.
DR BioGRID; 122377; 38.
DR CORUM; Q9H902; -.
DR IntAct; Q9H902; 18.
DR STRING; 9606.ENSP00000438346; -.
DR TCDB; 8.A.108.1.8; the curvature-stabilizing protein yop1 (yop1) family.
DR iPTMnet; Q9H902; -.
DR PhosphoSitePlus; Q9H902; -.
DR BioMuta; REEP1; -.
DR DMDM; 74733929; -.
DR MassIVE; Q9H902; -.
DR MaxQB; Q9H902; -.
DR PaxDb; Q9H902; -.
DR PeptideAtlas; Q9H902; -.
DR PRIDE; Q9H902; -.
DR ProteomicsDB; 81261; -. [Q9H902-1]
DR ProteomicsDB; 81262; -. [Q9H902-2]
DR ProteomicsDB; 81263; -. [Q9H902-3]
DR ProteomicsDB; 81264; -. [Q9H902-4]
DR Antibodypedia; 32091; 252 antibodies from 27 providers.
DR DNASU; 65055; -.
DR Ensembl; ENST00000165698.9; ENSP00000165698.5; ENSG00000068615.20. [Q9H902-1]
DR Ensembl; ENST00000453231.6; ENSP00000392197.2; ENSG00000068615.20. [Q9H902-3]
DR Ensembl; ENST00000535845.6; ENSP00000437567.1; ENSG00000068615.20. [Q9H902-2]
DR Ensembl; ENST00000541910.6; ENSP00000442681.1; ENSG00000068615.20. [Q9H902-4]
DR GeneID; 65055; -.
DR KEGG; hsa:65055; -.
DR UCSC; uc002srh.5; human. [Q9H902-1]
DR CTD; 65055; -.
DR DisGeNET; 65055; -.
DR GeneCards; REEP1; -.
DR HGNC; HGNC:25786; REEP1.
DR HPA; ENSG00000068615; Tissue enhanced (brain, testis).
DR MalaCards; REEP1; -.
DR MIM; 609139; gene.
DR MIM; 610250; phenotype.
DR MIM; 614751; phenotype.
DR neXtProt; NX_Q9H902; -.
DR OpenTargets; ENSG00000068615; -.
DR Orphanet; 101011; Autosomal dominant spastic paraplegia type 31.
DR Orphanet; 139536; Distal hereditary motor neuropathy type 5.
DR PharmGKB; PA134906680; -.
DR VEuPathDB; HostDB:ENSG00000068615; -.
DR eggNOG; KOG1726; Eukaryota.
DR GeneTree; ENSGT00940000159532; -.
DR HOGENOM; CLU_028431_0_2_1; -.
DR InParanoid; Q9H902; -.
DR PhylomeDB; Q9H902; -.
DR TreeFam; TF314177; -.
DR PathwayCommons; Q9H902; -.
DR Reactome; R-HSA-9752946; Expression and translocation of olfactory receptors.
DR SignaLink; Q9H902; -.
DR BioGRID-ORCS; 65055; 23 hits in 1069 CRISPR screens.
DR ChiTaRS; REEP1; human.
DR GeneWiki; REEP1; -.
DR GenomeRNAi; 65055; -.
DR Pharos; Q9H902; Tbio.
DR PRO; PR:Q9H902; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H902; protein.
DR Bgee; ENSG00000068615; Expressed in dorsal root ganglion and 200 other tissues.
DR ExpressionAtlas; Q9H902; baseline and differential.
DR Genevisible; Q9H902; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0031849; F:olfactory receptor binding; IMP:HGNC-UCL.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; IDA:HGNC-UCL.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Hereditary spastic paraplegia; Membrane; Mitochondrion; Neurodegeneration;
KW Neuropathy; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..201
FT /note="Receptor expression-enhancing protein 1"
FT /id="PRO_0000101821"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 158..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..35
FT /note="MVSWIISRLVVLIFGTLYPAYYSYKAVKSKDIKEY -> MDHLQAGG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042573"
FT VAR_SEQ 1..11
FT /note="MVSWIISRLVV -> MQKVLSNGQTEEVRSGSR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043251"
FT VAR_SEQ 62..201
FT /note="FPFYYELKIAFVAWLLSPYTKGSSLLYRKFVHPTLSSKEKEIDDCLVQAKDR
FT SYDALVHFGKRGLNVAATAAVMAASKGQGALSERLRSFSMQDLTTIRGDGAPAPSGPPP
FT PGSGRASGKHGQPKMSRSASESASSSGTA -> DRVPYRRDCGASACRTSPPSGETAPL
FT LPRAPHHRGLGGPAANTASLRCPGVLLRALAAQAPPRILRSRFRKKSTSSSATETT
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043252"
FT VARIANT 19
FT /note="P -> L (in SPG31; impairs normal ER-targeting)"
FT /evidence="ECO:0000269|PubMed:21618648,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_067265"
FT VARIANT 19
FT /note="P -> R (in SPG31; impairs normal ER-targeting;
FT dbSNP:rs1060503496)"
FT /evidence="ECO:0000269|PubMed:24478229"
FT /id="VAR_072609"
FT VARIANT 20
FT /note="A -> E (in SPG31; loss of function mutation; shows
FT severely altered localization to numerous punctate small
FT structures throughout the cytoplasm; does not localize to
FT the endoplasmic reticulum; impairs normal ER targeting;
FT dbSNP:rs121918262)"
FT /evidence="ECO:0000269|PubMed:16826527,
FT ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:22703882,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_027351"
FT VARIANT 23
FT /note="S -> F (in SPG31; impairs normal ER-targeting)"
FT /evidence="ECO:0000269|PubMed:21618648,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_067266"
FT VARIANT 42
FT /note="W -> R (in SPG31; impairs normal ER-targeting)"
FT /evidence="ECO:0000269|PubMed:21618648,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_067267"
FT VARIANT 55
FT /note="T -> K (in SPG31; unknown pathological significance;
FT does not impair normal ER-targeting)"
FT /evidence="ECO:0000269|PubMed:18644145,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_072610"
FT VARIANT 56
FT /note="D -> N (in SPG31; unknown pathological significance;
FT does not impair normal ER-targeting; dbSNP:rs1060503493)"
FT /evidence="ECO:0000269|PubMed:21618648,
FT ECO:0000269|PubMed:24478229"
FT /id="VAR_067268"
FT VARIANT 107
FT /note="L -> P (in SPG31)"
FT /evidence="ECO:0000269|PubMed:18644145"
FT /id="VAR_072611"
SQ SEQUENCE 201 AA; 22255 MW; 98F120DE100276A9 CRC64;
MVSWIISRLV VLIFGTLYPA YYSYKAVKSK DIKEYVKWMM YWIIFALFTT AETFTDIFLC
WFPFYYELKI AFVAWLLSPY TKGSSLLYRK FVHPTLSSKE KEIDDCLVQA KDRSYDALVH
FGKRGLNVAA TAAVMAASKG QGALSERLRS FSMQDLTTIR GDGAPAPSGP PPPGSGRASG
KHGQPKMSRS ASESASSSGT A
